Characterization of functional domains of the tenascin-R (restrictin) 
polypeptide: cell attachment site, binding with F11, and enhancement of 
F11-mediated neurite outgrowth by tenascin-R

Nörenberg, U; Hubert, M; Brümmendorf, T; Tárnok, A; Rathjen, FG

doi:10.1083/jcb.130.2.473

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Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R

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Brümmendorf, T
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Nörenberg, U., Hubert, M., Brümmendorf, T., Tárnok, A., & Rathjen, F. (1995). Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R. Journal of Cell Biology, 130(2), 473-484. doi:10.1083/jcb.130.2.473.

Cite as: https://hdl.handle.net/21.11116/0000-000D-97FD-C

Abstract

The extracellular matrix glycoprotein tenascin-R (TN-R) is a multidomain protein implicated in neural cell adhesion. To analyze the structure-function relationship of the different domains of TN-R, several recombinant TN-R fragments were expressed in bacterial cells. Two distinct binding regions were localized on the TN-R polypeptide: a region binding the axon-associated immunoglobulin (Ig)-like F11 protein and a cell attachment site. The binding region of the glycosylphosphatidylinositol (GPI)-anchored F11 was allocated to the second and third fibronectin type III (FNIII)-like domain within TN-R. By using a mutant polypeptide of F11 containing only Ig-like domains, a direct interaction between the Ig-like domains of F11 and FNIII-like domains 2-3 of TN-R was demonstrated. The interaction of TN-R with F11 in in vitro cultures enhanced F11-mediated neurite outgrowth, suggesting that the combined action of F11 and TN-R might be of regulatory influence on axon extension. A cell attachment region was identified in the FNIII-like domain eight of TN-R by domain-specific antibodies and fusion constructs. This site is distinct from the F11 binding site within TN-R.